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CAZyme Information: MGYG000002101_00708

You are here: Home > Sequence: MGYG000002101_00708

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Sutterella seckii_A
Lineage Bacteria; Proteobacteria; Gammaproteobacteria; Burkholderiales; Burkholderiaceae; Sutterella; Sutterella seckii_A
CAZyme ID MGYG000002101_00708
CAZy Family CBM50
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
300 31235.86 10.0968
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002101 2568007 MAG Mongolia Asia
Gene Location Start: 28634;  End: 29536  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002101_00708.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
PRK10871 nlpD 1.80e-45 13 296 16 317
murein hydrolase activator NlpD.
COG0739 NlpD 1.13e-44 61 299 3 268
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contain LysM domain [Cell wall/membrane/envelope biogenesis].
pfam01551 Peptidase_M23 3.24e-32 199 291 4 96
Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.
COG4942 EnvC 7.39e-25 120 291 239 414
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning].
cd12797 M23_peptidase 1.22e-24 199 282 2 85
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins. This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
QDA55742.1 4.48e-182 1 300 1 295
QQS89964.1 8.43e-99 16 299 15 312
BBF24071.1 9.85e-90 17 299 36 323
QBR40763.1 7.62e-52 15 296 16 285
AZV93835.1 1.07e-51 15 296 16 285

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4BH5_A 1.81e-15 178 295 17 140
LytMdomain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_B LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_C LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12],4BH5_D LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli [Escherichia coli K-12]
6TPI_A 4.30e-14 178 295 261 384
EnvCbound to the FtsX periplasmic domain [Escherichia coli K-12]
5J1L_A 1.80e-08 189 294 57 163
Crystalstructure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1L_C Crystal structure of Csd1-Csd2 dimer I [Helicobacter pylori 26695],5J1M_A Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695],5J1M_C Crystal structure of Csd1-Csd2 dimer II [Helicobacter pylori 26695]
4UZ2_A 2.14e-08 60 109 3 51
Crystalstructure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ2_D Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4UZ3_A Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_B Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8],4UZ3_C Crystal structure of the N-terminal LysM domains from the putative NlpC/P60 D,L endopeptidase from T. thermophilus bound to N-acetyl-chitohexaose [Thermus thermophilus HB8]
4XCM_A 1.15e-06 60 109 3 51
Crystalstructure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8],4XCM_B Crystal structure of the putative NlpC/P60 D,L endopeptidase from T. thermophilus [Thermus thermophilus HB8]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P45682 1.80e-46 19 296 34 295
Lipoprotein NlpD/LppB homolog OS=Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) OX=208964 GN=PA3623 PE=3 SV=1
Q46798 7.07e-40 58 297 38 244
Uncharacterized lipoprotein YgeR OS=Escherichia coli (strain K12) OX=83333 GN=ygeR PE=3 SV=2
P44833 1.72e-34 59 296 144 403
Outer membrane antigenic lipoprotein B OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=lppB PE=3 SV=1
P0ADA3 2.17e-33 58 296 119 377
Murein hydrolase activator NlpD OS=Escherichia coli (strain K12) OX=83333 GN=nlpD PE=1 SV=1
P0ADA4 2.17e-33 58 296 119 377
Murein hydrolase activator NlpD OS=Shigella flexneri OX=623 GN=nlpD PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000002 1.000013 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002101_00708.